Native Thrombocidin-1 and Unfolded Thrombocidin-1 Exert Antimicrobial Activity via Distinct Structural Elements-Reference-Cited by-同舟云学术

Native Thrombocidin-1 and Unfolded Thrombocidin-1 Exert Antimicrobial Activity via Distinct Structural Elements

Published:2011-12 Issue:50 Volume:286 Page:43506-43514
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kwakman Paulus H.S.,Krijgsveld Jeroen,de Boer Leonie,Nguyen Leonard T.,Boszhard Laura,Vreede Jocelyne,Dekker Henk L.,Speijer Dave,Drijfhout Jan W.,te Velde Anje A.,Crielaard Wim,Vogel Hans J.,Vandenbroucke-Grauls Christina M.J.E.,Zaat Sebastian A.J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

1. Structure, Function, and Inhibition of Chemokines

2. Thrombocidins, Microbicidal Proteins from Human Blood Platelets, Are C-terminal Deletion Products of CXC Chemokines

3. Cutting Edge: IFN-Inducible ELR−CXC Chemokines Display Defensin-Like Antimicrobial Activity

4. Many chemokines including CCL20/MIP-3α display antimicrobial activity

5. The Structure of Human Macrophage Inflammatory Protein-3α/CCL20

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